1993
DOI: 10.1021/bi00095a012 View full text |Buy / Rent full text
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Abstract: The near-UV absorption and fluorescence spectroscopic properties of Trp-3 of pig pancreatic phospholipase A2 (PLA2) in aqueous solution (E form) or at the interface without (E* form) or with a ligand at the active site (E*L form) are characterized. In the E form, the single tryptophan residue is exposed on the protein surface to the aqueous environment, as it is freely accessible to aqueous quenchers such as succinimide and acrylamide. The fluorescence quantum yield of E is about one-third that of N-acetyl-try… Show more

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“…31 Also, binding of PLA 2 to micelles of hexadecyl-propanediolphosphocholine resulted in substantial (O15-fold) decrease in the accessibility of succinimide to Trp3. 32 These findings, together with preferential quenching of Trp3 by bromine at the C9-C11 positions of lipids or fatty acids 30 are consistent with insertion of Trp3 half-way to the membrane center. Furthermore, Jain and Vaz have measured the efficiency of energy transfer between Trp3 of membrane-bound porcine pancreatic PLA 2 and the dansyl chromophore attached to the headgroup of hexadecyl-phosphorylethanolamine in anionic membranes to be E O0.95, which was used to estimate a distance between Trp3 and the membrane surface rz8 Å using a Fö rster distance of R o Z17-18 Å for the Trp-dansyl pair.…”
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“…31 Also, binding of PLA 2 to micelles of hexadecyl-propanediolphosphocholine resulted in substantial (O15-fold) decrease in the accessibility of succinimide to Trp3. 32 These findings, together with preferential quenching of Trp3 by bromine at the C9-C11 positions of lipids or fatty acids 30 are consistent with insertion of Trp3 half-way to the membrane center. Furthermore, Jain and Vaz have measured the efficiency of energy transfer between Trp3 of membrane-bound porcine pancreatic PLA 2 and the dansyl chromophore attached to the headgroup of hexadecyl-phosphorylethanolamine in anionic membranes to be E O0.95, which was used to estimate a distance between Trp3 and the membrane surface rz8 Å using a Fö rster distance of R o Z17-18 Å for the Trp-dansyl pair.…”
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“…Several spectroscopic studies also identified conformational changes in group IB and IIA PLA 2 s upon binding to phospholipid micelles or membranes. Fluorescence studies indicated that the N-terminal helix of porcine group IB PLA 2 becomes rigid upon enzyme-substrate complex formation at the membrane surface (9,10). This was confirmed by NMR experiments, which indicated that the N-terminal ␣-helix and H-bonded catalytically important residues of porcine group IB PLA 2 were flexible in the aqueous buffer and adopted a fixed conformation in a ternary complex of the enzyme with a substrate analog and phospholipid micelles (11,12).…”
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“…These conformational changes have not affected the binding of the enzyme to the interface. There is no evidence from the fluorescence binding studies ( Jain & Maliwal, 1993) of any substantial change in the substrate binding of the enzyme to the interface (M.K. Jain, unpubl.…”
Section: A Kumar Et Almentioning